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- EMDB-16036: human MDM2-5S RNP -

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Basic information

Entry
Database: EMDB / ID: EMD-16036
Titlehuman MDM2-5S RNP
Map datahuman MDM2-5S RNP (local filtered map)
Sample
  • Complex: human MDM2-5S RNP
    • Protein or peptide: E3 ubiquitin-protein ligase Mdm2
    • RNA: 5S rRNA
    • Protein or peptide: 60S ribosomal protein L5
    • Protein or peptide: 60S ribosomal protein L11
  • Ligand: ZINC ION
Keywords5S RNP / Mdm2 / RNA BINDING PROTEIN
Function / homology
Function and homology information


cellular response to vitamin B1 / response to formaldehyde / response to water-immersion restraint stress / traversing start control point of mitotic cell cycle / negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator / response to ether / negative regulation of signal transduction by p53 class mediator / fibroblast activation / atrial septum development / negative regulation of protein neddylation ...cellular response to vitamin B1 / response to formaldehyde / response to water-immersion restraint stress / traversing start control point of mitotic cell cycle / negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator / response to ether / negative regulation of signal transduction by p53 class mediator / fibroblast activation / atrial septum development / negative regulation of protein neddylation / receptor serine/threonine kinase binding / Trafficking of AMPA receptors / positive regulation of vascular associated smooth muscle cell migration / peroxisome proliferator activated receptor binding / SUMO transferase activity / negative regulation of protein processing / response to iron ion / response to steroid hormone / NEDD8 ligase activity / AKT phosphorylates targets in the cytosol / atrioventricular valve morphogenesis / cellular response to peptide hormone stimulus / ventricular septum development / endocardial cushion morphogenesis / negative regulation of ubiquitin protein ligase activity / positive regulation of muscle cell differentiation / SUMOylation of ubiquitinylation proteins / cellular response to alkaloid / blood vessel development / regulation of protein catabolic process / cardiac septum morphogenesis / Constitutive Signaling by AKT1 E17K in Cancer / Peptide chain elongation / ligase activity / Selenocysteine synthesis / positive regulation of signal transduction by p53 class mediator / negative regulation of DNA damage response, signal transduction by p53 class mediator / ubiquitin ligase inhibitor activity / Formation of a pool of free 40S subunits / response to magnesium ion / Eukaryotic Translation Termination / SUMOylation of transcription factors / Response of EIF2AK4 (GCN2) to amino acid deficiency / protein sumoylation / SRP-dependent cotranslational protein targeting to membrane / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Viral mRNA Translation / protein localization to nucleus / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / L13a-mediated translational silencing of Ceruloplasmin expression / GTP hydrolysis and joining of the 60S ribosomal subunit / cellular response to UV-C / Major pathway of rRNA processing in the nucleolus and cytosol / blood vessel remodeling / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / cellular response to estrogen stimulus / protein targeting / protein autoubiquitination / cellular response to actinomycin D / ribonucleoprotein complex binding / cytosolic ribosome / positive regulation of vascular associated smooth muscle cell proliferation / DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest / NPAS4 regulates expression of target genes / transcription repressor complex / regulation of heart rate / negative regulation of ubiquitin-dependent protein catabolic process / positive regulation of mitotic cell cycle / positive regulation of protein export from nucleus / response to cocaine / proteolysis involved in protein catabolic process / regulation of signal transduction by p53 class mediator / ribosomal large subunit biogenesis / ubiquitin binding / mRNA 3'-UTR binding / positive regulation of translation / Stabilization of p53 / Regulation of RUNX3 expression and activity / protein destabilization / RING-type E3 ubiquitin transferase / establishment of protein localization / Oncogene Induced Senescence / Regulation of TP53 Activity through Methylation / ribosomal large subunit assembly / response to toxic substance / cellular response to gamma radiation / cellular response to growth factor stimulus / mRNA 5'-UTR binding / Regulation of expression of SLITs and ROBOs / cellular response to hydrogen peroxide / protein polyubiquitination / rRNA processing / ubiquitin-protein transferase activity / endocytic vesicle membrane / ubiquitin protein ligase activity / disordered domain specific binding / Signaling by ALK fusions and activated point mutants / Regulation of TP53 Degradation / p53 binding / positive regulation of proteasomal ubiquitin-dependent protein catabolic process
Similarity search - Function
E3 ubiquitin-protein ligase Mdm2 / MDM2, modified RING finger, HC subclass / p53 negative regulator Mdm2/Mdm4 / SWIB/MDM2 domain / SWIB/MDM2 domain / SWIB/MDM2 domain profile. / SWIB/MDM2 domain superfamily / Zn-finger in Ran binding protein and others / Zinc finger, C3HC4 type (RING finger) / Zinc finger RanBP2 type profile. ...E3 ubiquitin-protein ligase Mdm2 / MDM2, modified RING finger, HC subclass / p53 negative regulator Mdm2/Mdm4 / SWIB/MDM2 domain / SWIB/MDM2 domain / SWIB/MDM2 domain profile. / SWIB/MDM2 domain superfamily / Zn-finger in Ran binding protein and others / Zinc finger, C3HC4 type (RING finger) / Zinc finger RanBP2 type profile. / Zinc finger RanBP2-type signature. / Zinc finger, RanBP2-type superfamily / Zinc finger, RanBP2-type / Ribosomal protein L5 eukaryotic, C-terminal / Ribosomal L18 C-terminal region / Ribosomal protein L5 eukaryotic/L18 archaeal / Ribosomal large subunit proteins 60S L5, and 50S L18 / Zinc finger RING-type profile. / Zinc finger, RING-type / Ribosomal protein L5, conserved site / Ribosomal protein L5 signature. / Ribosomal protein L5, N-terminal / Ribosomal protein L5 / Ribosomal protein L5, C-terminal / ribosomal L5P family C-terminus / Ribosomal protein L5 / Ribosomal protein L5 domain superfamily / Zinc finger, RING/FYVE/PHD-type
Similarity search - Domain/homology
Large ribosomal subunit protein uL18 / Large ribosomal subunit protein uL5 / E3 ubiquitin-protein ligase Mdm2
Similarity search - Component
Biological speciesHomo sapiens (human) / Saccharomyces cerevisiae (brewer's yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.1 Å
AuthorsCastillo N / Thoms M / Flemming D / Hammaren HM / Buschauer R / Ameismeier M / Bassler J / Beck M / Beckmann R / Hurt E
Funding support Germany, European Union, 3 items
OrganizationGrant numberCountry
German Research Foundation (DFG)RK1721 Germany
German Research Foundation (DFG)HU363/15-2 Germany
European Research Council (ERC)885711European Union
CitationJournal: Nat Struct Mol Biol / Year: 2023
Title: Structure of nascent 5S RNPs at the crossroad between ribosome assembly and MDM2-p53 pathways.
Authors: Nestor Miguel Castillo Duque de Estrada / Matthias Thoms / Dirk Flemming / Henrik M Hammaren / Robert Buschauer / Michael Ameismeier / Jochen Baßler / Martin Beck / Roland Beckmann / Ed Hurt /
Abstract: The 5S ribonucleoprotein (RNP) is assembled from its three components (5S rRNA, Rpl5/uL18 and Rpl11/uL5) before being incorporated into the pre-60S subunit. However, when ribosome synthesis is ...The 5S ribonucleoprotein (RNP) is assembled from its three components (5S rRNA, Rpl5/uL18 and Rpl11/uL5) before being incorporated into the pre-60S subunit. However, when ribosome synthesis is disturbed, a free 5S RNP can enter the MDM2-p53 pathway to regulate cell cycle and apoptotic signaling. Here we reconstitute and determine the cryo-electron microscopy structure of the conserved hexameric 5S RNP with fungal or human factors. This reveals how the nascent 5S rRNA associates with the initial nuclear import complex Syo1-uL18-uL5 and, upon further recruitment of the nucleolar factors Rpf2 and Rrs1, develops into the 5S RNP precursor that can assemble into the pre-ribosome. In addition, we elucidate the structure of another 5S RNP intermediate, carrying the human ubiquitin ligase Mdm2, which unravels how this enzyme can be sequestered from its target substrate p53. Our data provide molecular insight into how the 5S RNP can mediate between ribosome biogenesis and cell proliferation.
History
DepositionOct 28, 2022-
Header (metadata) releaseJun 14, 2023-
Map releaseJun 14, 2023-
UpdateAug 30, 2023-
Current statusAug 30, 2023Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_16036.png

Downloads & links

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Map

FileDownload / File: emd_16036.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationhuman MDM2-5S RNP (local filtered map)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 200 pix.
= 211.8 Å		1.06 Å/pix.
x 200 pix.
= 211.8 Å		1.06 Å/pix.
x 200 pix.
= 211.8 Å

Surface

Projections

Slices (1/3)

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Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.059 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.04
Minimum - Maximum-0.05936509 - 0.14046915
Average (Standard dev.)0.0003764116 (±0.0054293275)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions200200200
Spacing200200200
CellA=B=C: 211.8 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: human MDM2-5S RNP (post-processed map)

Fileemd_16036_additional_1.map
Annotationhuman MDM2-5S RNP (post-processed map)
Projections & Slices
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Additional map: human MDM2-5S RNP (maked 3D Refinement)

Fileemd_16036_additional_2.map
Annotationhuman MDM2-5S RNP (maked 3D Refinement)
Projections & Slices
AxesZYX

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Histogram

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Additional map: human MDM2-5S RNP (unmaked 3D Refinement)

Fileemd_16036_additional_3.map
Annotationhuman MDM2-5S RNP (unmaked 3D Refinement)
Projections & Slices
AxesZYX

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Histogram

Histogram (log scale)

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Half map: human MDM2-5S RNP (maked 3D Refinement, half map 1)

Fileemd_16036_half_map_1.map
Annotationhuman MDM2-5S RNP (maked 3D Refinement, half map 1)
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Half map: human MDM2-5S RNP (maked 3D Refinement, half map 2)

Fileemd_16036_half_map_2.map
Annotationhuman MDM2-5S RNP (maked 3D Refinement, half map 2)
Projections & Slices
AxesZYX

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Histogram

Histogram (log scale)

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Sample components

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Entire : human MDM2-5S RNP

EntireName: human MDM2-5S RNP
Components
  • Complex: human MDM2-5S RNP
    • Protein or peptide: E3 ubiquitin-protein ligase Mdm2
    • RNA: 5S rRNA
    • Protein or peptide: 60S ribosomal protein L5
    • Protein or peptide: 60S ribosomal protein L11
  • Ligand: ZINC ION

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Supramolecule #1: human MDM2-5S RNP

SupramoleculeName: human MDM2-5S RNP / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: E3 ubiquitin-protein ligase Mdm2

MacromoleculeName: E3 ubiquitin-protein ligase Mdm2 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: RING-type E3 ubiquitin transferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 55.293758 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MCNTNMSVPT DGAVTTSQIP ASEQETLVRP KPLLLKLLKS VGAQKDTYTM KEVLFYLGQY IMTKRLYDEK QQHIVYCSND LLGDLFGVP SFSVKEHRKI YTMIYRNLVV VNQQESSDSG TSVSENRCHL EGGSDQKDLV QELQEEKPSS SHLVSRPSTS S RRRAISET ...String:
MCNTNMSVPT DGAVTTSQIP ASEQETLVRP KPLLLKLLKS VGAQKDTYTM KEVLFYLGQY IMTKRLYDEK QQHIVYCSND LLGDLFGVP SFSVKEHRKI YTMIYRNLVV VNQQESSDSG TSVSENRCHL EGGSDQKDLV QELQEEKPSS SHLVSRPSTS S RRRAISET EENSDELSGE RQRKRHKSDS ISLSFDESLA LCVIREICCE RSSSSESTGT PSNPDLDAGV SEHSGDWLDQ DS VSDQFSV EFEVESLDSE DYSLSEEGQE LSDEDDEVYQ VTVYQAGESD TDSFEEDPEI SLADYWKCTS CNEMNPPLPS HCN RCWALR ENWLPEDKGK DKGEISEKAK LENSTQAEEG FDVPDCKKTI VNDSRESCVE ENDDKITQAS QSQESEDYSQ PSTS SSIIY SSQEDVKEFE REETQDKEES VESSLPLNAI EPCVICQGRP KNGCIVHGKT GHLMACFTCA KKLKKRNKPC PVCRQ PIQM IVLTYFP

UniProtKB: E3 ubiquitin-protein ligase Mdm2

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Macromolecule #3: 60S ribosomal protein L5

MacromoleculeName: 60S ribosomal protein L5 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 34.426789 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MGFVKVVKNK AYFKRYQVKF RRRREGKTDY YARKRLVIQD KNKYNTPKYR MIVRVTNRDI ICQIAYARIE GDMIVCAAYA HELPKYGVK VGLTNYAAAY CTGLLLARRL LNRFGMDKIY EGQVEVTGDE YNVESIDGQP GAFTCYLDAG LARTTTGNKV F GALKGAVD ...String:
MGFVKVVKNK AYFKRYQVKF RRRREGKTDY YARKRLVIQD KNKYNTPKYR MIVRVTNRDI ICQIAYARIE GDMIVCAAYA HELPKYGVK VGLTNYAAAY CTGLLLARRL LNRFGMDKIY EGQVEVTGDE YNVESIDGQP GAFTCYLDAG LARTTTGNKV F GALKGAVD GGLSIPHSTK RFPGYDSESK EFNAEVHRKH IMGQNVADYM RYLMEEDEDA YKKQFSQYIK NSVTPDMMEE MY KKAHAAI RENPVYEKKP KKEVKKKRWN RPKMSLAQKK DRVAQKKASF LRAQERAAES

UniProtKB: Large ribosomal subunit protein uL18

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Macromolecule #4: 60S ribosomal protein L11

MacromoleculeName: 60S ribosomal protein L11 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 20.288465 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
MAQDQGEKEN PMRELRIRKL CLNICVGESG DRLTRAAKVL EQLTGQTPVF SKARYTVRSF GIRRNEKIAV HCTVRGAKAE EILEKGLKV REYELRKNNF SDTGNFGFGI QEHIDLGIKY DPSIGIYGLD FYVVLGRPGF SIADKKRRTG CIGAKHRISK E EAMRWFQQ KYDGIILPGK

UniProtKB: Large ribosomal subunit protein uL5

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Macromolecule #2: 5S rRNA

MacromoleculeName: 5S rRNA / type: rna / ID: 2 / Number of copies: 1
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 38.951105 KDa
SequenceString:
GGUUGCGGCC AUAUCUACCA GAAAGCACCG UUUCCCGUCC GAUCAACUGU AGUUAAGCUG GUAAGAGCCU GACCGAGUAG UGUAGUGGG UGACCAUACG CGAAACUCAG GUGCUGCAAU CU

GENBANK: GENBANK: CP008196.1

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Macromolecule #5: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 5 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
GridMaterial: GOLD
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 38.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 4.0 µm / Nominal defocus min: 0.4 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 219620
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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